ID G5JYQ0_9STRE Unreviewed; 404 AA.
AC G5JYQ0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=FemAB family protein {ECO:0000313|EMBL:EHJ52672.1};
GN ORFNames=STRMA_0313 {ECO:0000313|EMBL:EHJ52672.1};
OS Streptococcus macacae NCTC 11558.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764298 {ECO:0000313|EMBL:EHJ52672.1, ECO:0000313|Proteomes:UP000003573};
RN [1] {ECO:0000313|EMBL:EHJ52672.1, ECO:0000313|Proteomes:UP000003573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 11558 {ECO:0000313|EMBL:EHJ52672.1,
RC ECO:0000313|Proteomes:UP000003573};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00008694}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ52672.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEUW02000001; EHJ52672.1; -; Genomic_DNA.
DR RefSeq; WP_003080967.1; NZ_UHFV01000002.1.
DR AlphaFoldDB; G5JYQ0; -.
DR STRING; 764298.STRMA_0313; -.
DR eggNOG; COG2348; Bacteria.
DR OrthoDB; 2173585at2; -.
DR Proteomes; UP000003573; Unassembled WGS sequence.
DR GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.90; -; 1.
DR Gene3D; 3.40.630.30; -; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003447; FEMABX.
DR PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR PANTHER; PTHR36174:SF1; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR Pfam; PF02388; FemAB; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR PROSITE; PS51191; FEMABX; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT COILED 237..290
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 404 AA; 46629 MW; FCB34C12BF0A924B CRC64;
MYTYKVGISQ EEHDHFIKNS SQTNLLQSSS WAKVKNEWGN ERIGFYQDGQ LVASASILIR
SLPLGMTMFY IPRGPVMDYQ NKDLVNFVLS SLKKIAKRKR ALFIKFDPFI LLNHHQIDKE
AIDNPQAQDI INNLKNLGCE WLGQTTDMGE NIQPRFQANI YADGFTEENL SKKIRQSIRT
AKNKGVMIQF GDDDLLEDFA FLMKKTEDRK SIHLRGIDYY RKLLDSYPKQ SFITLASLNL
AERLAELEKQ KEKAQNNLAK FGDNVKPSKI DNTKKEIERL SDEIAFLQEH LSQGNEIVPL
SGTLSLEFGG TSENIYAGMD EEFRRYQAAI YTWFETARHA FDRGNIWQNM GGVENDLSGG
LYHFKSKFKP EIEEFIGEFN LPVSPLYHLA NIAYTIRKKR RSKH
//
